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- PDB-1r48: Solution structure of the C-terminal cytoplasmic domain residues ... -

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Basic information

Entry
Database: PDB / ID: 1r48
TitleSolution structure of the C-terminal cytoplasmic domain residues 468-497 of Escherichia coli protein ProP
ComponentsProline/betaine transporter
KeywordsTRANSPORT PROTEIN / OSMOSENSOR / CYTOPLASMIC / COILED-COIL / ANTIPARALLEL / TWO-STRANDED HOMODIMER
Function / homology
Function and homology information


proline:proton symporter activity / proline import across plasma membrane / glycine betaine transport / osmosensory signaling pathway / cellular hyperosmotic response / cellular hyperosmotic salinity response / amino acid transport / membrane => GO:0016020 / protein homodimerization activity / plasma membrane
Similarity search - Function
MFS transporter, metabolite:H symporter / Osmosensory transporter coiled coil / Proline/betaine transporter ProP, C-terminal / : / Osmosensory transporter coiled coil / Sugar transport proteins signature 1. / Sugar transporter, conserved site / Major facilitator, sugar transporter-like / Sugar (and other) transporter / Major facilitator superfamily domain ...MFS transporter, metabolite:H symporter / Osmosensory transporter coiled coil / Proline/betaine transporter ProP, C-terminal / : / Osmosensory transporter coiled coil / Sugar transport proteins signature 1. / Sugar transporter, conserved site / Major facilitator, sugar transporter-like / Sugar (and other) transporter / Major facilitator superfamily domain / Major facilitator superfamily (MFS) profile. / MFS transporter superfamily
Similarity search - Domain/homology
Proline/betaine transporter / Proline/betaine transporter
Similarity search - Component
MethodSOLUTION NMR / simulated annealing
Model type detailsminimized average
AuthorsZoetewey, D.L. / Tripet, B.P. / Kutateladze, T.G. / Overduin, M.J. / Wood, J.M. / Hodges, R.S.
CitationJournal: J.Mol.Biol. / Year: 2003
Title: Solution Structure of the C-terminal Antiparallel Coiled-coil Domain from Escherichia coli Osmosensor ProP.
Authors: Zoetewey, D.L. / Tripet, B.P. / Kutateladze, T.G. / Overduin, M.J. / Wood, J.M. / Hodges, R.S.
History
DepositionOct 3, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 23, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Proline/betaine transporter
B: Proline/betaine transporter


Theoretical massNumber of molelcules
Total (without water)7,6402
Polymers7,6402
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)51 / 63structures with favorable non-bond energy
RepresentativeModel #1minimized average structure

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Components

#1: Protein/peptide Proline/betaine transporter / Proline porter II / PPII


Mass: 3820.233 Da / Num. of mol.: 2 / Fragment: C-TERMINAL DOMAIN (residue 468-497) / Source method: obtained synthetically
Details: Synthetic peptide including a CGG N-terminal linker blocked with iodoacetamide, N-terminally acetylated, C-terminally amidated. This sequence is naturally present in Escherichia coli.
References: UniProt: P30848, UniProt: P0C0L7*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
2112D NOESY
2212D TOCSY
231DQF-COSY

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Sample preparation

DetailsContents: 2 mM Unlabled peptide ProP 468-497, 50 mM potassium phosphate, 100 mM KCl, 90% H2O, 10% D2O, 1 mM NaN3
Solvent system: 90% H20, 10% D2O
Sample conditionsIonic strength: 150 mM / pH: 5 / Pressure: ambient / Temperature: 293 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
CNS1.1Brunger, Adams, Clore, Delano, Gros, Grosse-Kunstleve, Jiang, Kuszewski, Nilges, Pannu, Read, Rice, Simonson, Warrenstructure solution
CNS1.1Brunger, Adams, Clore, Delano, Gros, Grosse-Kunstleve, Jiang, Kuszewski, Nilges, Pannu, Read, Rice, Simonson, Warrenrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
Details: The structures are based on 676 total restraints, 632 NOE-derived distance constraints and 44 Hydrogen-bond distance restraints.
NMR representativeSelection criteria: minimized average structure
NMR ensembleConformer selection criteria: structures with favorable non-bond energy
Conformers calculated total number: 63 / Conformers submitted total number: 51

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